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Virus-like particles (VLPs) are nanoscale structures formed by the self-assembly of viral structural proteins. Due to their morphology and immunogenicity, which resemble natural viruses but lack viral genetic material (DNA or RNA), VLPs are non-infectious and incapable of replication. As a powerful immunization platform, VLPs can significantly enhance immune responses through multivalent antigen presentation, making them particularly suitable for the development of vaccines against weak immunogens.
VLPs were first identified in 1968 in the serum of patients with Down syndrome, leukemia , and hepatitis . With the advancement of recombinant protein technology, VLPs have been widely used in the fields of vaccinology, drug delivery, and diagnostics.
The reasons to choose VLPs:
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The structure of VLPs is formed by the self-assembly of viral capsid proteins. Based on their complexity and geometric symmetry, VLPs can be classified as follows:
Composed of one or more capsid proteins, these have a simple structure and are commonly found in vaccines for human papillomavirus (HPV).
These contain a lipid bilayer and embedded viral glycoproteins, with structures more similar to natural viruses. They are commonly found in vaccines for influenza and HIV.
VLPs can be produced using a variety of expression systems, each with its unique advantages and limitations.
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| VLP Production System | Advantages | Limitations | Application Cases |
| Bacterial Systems (e.g., E. coli) | - Low cost - Fast production - Suitable for non-enveloped VLPs | - Lack of post-translational modifications (e.g., glycosylation) - Not suitable for complex VLPs | - Hepatitis C vaccine - HPV vaccine (in clinical trials) |
| Yeast Systems (e.g., S. cerevisiae, P. pastoris) | - High protein yield - Partial post-translational modifications - Cost-effective | - Simple glycosylation pattern - Not suitable for some EVLPs | - Hepatitis B vaccine - HPV vaccine |
| Insect Cell-Baculovirus System (B/IC) | - High yield - Complex post-translational modifications - Suitable for EVLPs | - Glycosylation pattern may affect immunogenicity | - HPV vaccine - Influenza vaccine |
| Mammalian Cell Systems (e.g., CHO cells) | - Precise post-translational modifications (e.g., glycosylation) - Suitable for complex VLPs | - High cost - Long production cycle | - Hepatitis B vaccine - Dengue vaccine |
| Plant Expression Systems | - Low cost - High expression levels - Suitable for large-scale production | - Glycosylation pattern may affect stability | - Influenza vaccine - Norovirus vaccine |
| Cell-Free Protein Synthesis (CFPS) | - Fast - High protein yield - Can produce toxic proteins | - High cost - Limited scalability | - Influenza VLP vaccine - Hepatitis B vaccine |
VLPs have shown great potential in cancer immunotherapy , especially in cancer vaccine development and combination treatment strategies.
VLPs efficiently deliver tumor-associated antigens (TAAs) and tumor-specific antigens (TSAs) , triggering strong immune responses by activating B cells, DCs, and T cells. Moreover, VLPs can regulate the tumor microenvironment, breaking immune tolerance within tumors and enhancing anti-tumor immunity. These properties make VLPs suitable not only for cancer vaccine development but also for use in combination with chemotherapy or immune checkpoint inhibitors for more comprehensive treatment outcomes.
Currently, the application of VLPs in cancer immunotherapy has made significant progress. For example, HPV vaccines have been widely used for the prevention of cervical cancer caused by HPV infection, marking the successful application of VLPs in cancer prevention.
VLPs interact with pattern recognition receptors (PRRs) on dendritic cells (DCs) to activate the innate immune response:
Antigens displayed on the surface of VLPs can break B cell self-tolerance and induce tumor-specific B cell responses.
VLPs present antigens via MHC-I and MHC-II molecules, activating CD4+ and CD8+ T cells, enhancing cellular immune responses.
Several key challenges remain in realizing the potential of VLPs.
First, production costs are a major barrier, especially for mammalian and insect cell systems, where high costs limit their feasibility for large-scale use. Additionally, the stability of EVLPs remains a pressing issue, as their sensitivity to external conditions requires optimized storage and transportation conditions to ensure efficacy and reliability. Lastly, concerning immunogenicity, researchers need to further explore how the density and conformation of antigens presented on the surface of VLPs affect immune responses to design more efficient and precise vaccines and drug delivery systems.
These challenges will need to be addressed through technological innovation and research breakthroughs to drive the broad application of VLPs in the future.
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